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Protein

Protein translocase subunit SecY

Gene

secY

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.UniRule annotation

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciVCHO:VC2576-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecYUniRule annotation
Gene namesi
Name:secYUniRule annotation
Ordered Locus Names:VC_2576
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

  • Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei24 – 4421HelicalUniRule annotationAdd
BLAST
Transmembranei77 – 9721HelicalUniRule annotationAdd
BLAST
Transmembranei123 – 14321HelicalUniRule annotationAdd
BLAST
Transmembranei153 – 17321HelicalUniRule annotationAdd
BLAST
Transmembranei181 – 20121HelicalUniRule annotationAdd
BLAST
Transmembranei215 – 23521HelicalUniRule annotationAdd
BLAST
Transmembranei269 – 28921HelicalUniRule annotationAdd
BLAST
Transmembranei318 – 33821HelicalUniRule annotationAdd
BLAST
Transmembranei376 – 39621HelicalUniRule annotationAdd
BLAST
Transmembranei400 – 42021HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Protein translocase subunit SecYPRO_0000131758Add
BLAST

Interactioni

Subunit structurei

Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA.UniRule annotation

Protein-protein interaction databases

STRINGi243277.VC2576.

Structurei

3D structure databases

ProteinModelPortaliP78283.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SecY/SEC61-alpha family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CGG. Bacteria.
COG0201. LUCA.
KOiK03076.
OMAiQTYVISQ.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY. 1 hit.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR030659. SecY_CS.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKPGQDFR SAQSGLSELK SRLFFVIGAL LVFRAGSFVP IPGIDAAVLA
60 70 80 90 100
ELFEQQKGTI VEMFNMFSGG ALERASILAL GIMPYISASI VVQLLTVVHP
110 120 130 140 150
ALAELKKEGE AGRRKISQYT RYGTLVLATF QAIGIATGLP NMVNNLVVID
160 170 180 190 200
QTMFTLIATV SLVTGTMFLM WLGEQITERG IGNGISILIF AGIVAGLPKA
210 220 230 240 250
IGQTIEQARQ GELHVLLLLL IAVLAFAVIY FVVFMERGQR RIVVNYAKRQ
260 270 280 290 300
QGRKVFAAQS THLPLKINMA GVIPAIFASS IILFPGTLAQ WFGQNGESST
310 320 330 340 350
FGWLTDVSLA LSPGQPLYVM LYAAAIIFFC FFYTALVFNP RETADNLKKS
360 370 380 390 400
GAFVPGIRPG EQTAKYIDKV MTRLTLAGAL YITFICLIPE FMMVAWNVRF
410 420 430 440
YFGGTSLLIV VVVIMDFMAQ VQTHLMSHQY ESVLKKANLK GYGR
Length:444
Mass (Da):48,664
Last modified:December 1, 2000 - v2
Checksum:i9608C4FDB9FC89CF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171S → R in CAA69654 (PubMed:9322765).Curated
Sequence conflicti17 – 171S → R in CAA69151 (PubMed:9322765).Curated
Sequence conflicti82 – 821I → M in CAA69654 (PubMed:9322765).Curated
Sequence conflicti82 – 821I → M in CAA69151 (PubMed:9322765).Curated
Sequence conflicti103 – 1031Missing in CAA69654 (PubMed:9322765).Curated
Sequence conflicti103 – 1031Missing in CAA69151 (PubMed:9322765).Curated
Sequence conflicti140 – 1401P → R in CAA69654 (PubMed:9322765).Curated
Sequence conflicti140 – 1401P → R in CAA69151 (PubMed:9322765).Curated
Sequence conflicti208 – 2103Missing in CAA69654 (PubMed:9322765).Curated
Sequence conflicti208 – 2103Missing in CAA69151 (PubMed:9322765).Curated
Sequence conflicti233 – 2331V → L in CAA69654 (PubMed:9322765).Curated
Sequence conflicti233 – 2331V → L in CAA69151 (PubMed:9322765).Curated
Sequence conflicti278 – 2781A → C in CAA69654 (PubMed:9322765).Curated
Sequence conflicti278 – 2781A → C in CAA69151 (PubMed:9322765).Curated
Sequence conflicti297 – 3015ESSTF → AHS in CAA69654 (PubMed:9322765).Curated
Sequence conflicti297 – 3015ESSTF → AHS in CAA69151 (PubMed:9322765).Curated
Sequence conflicti343 – 3431T → S in CAA69654 (PubMed:9322765).Curated
Sequence conflicti343 – 3431T → S in CAA69151 (PubMed:9322765).Curated
Sequence conflicti388 – 3881I → N in CAA69654 (PubMed:9322765).Curated
Sequence conflicti388 – 3881I → N in CAA69151 (PubMed:9322765).Curated
Sequence conflicti399 – 3991R → P in CAA69654 (PubMed:9322765).Curated
Sequence conflicti399 – 3991R → P in CAA69151 (PubMed:9322765).Curated
Sequence conflicti417 – 4171F → L in CAA69654 (PubMed:9322765).Curated
Sequence conflicti417 – 4171F → L in CAA69151 (PubMed:9322765).Curated
Sequence conflicti421 – 4244VQTH → GTTL in CAA69654 (PubMed:9322765).Curated
Sequence conflicti421 – 4244VQTH → GTTL in CAA69151 (PubMed:9322765).Curated
Sequence conflicti437 – 4371A → D in CAA69654 (PubMed:9322765).Curated
Sequence conflicti437 – 4371A → D in CAA69151 (PubMed:9322765).Curated
Sequence conflicti442 – 4421Y → L in CAA69654 (PubMed:9322765).Curated
Sequence conflicti442 – 4421Y → L in CAA69151 (PubMed:9322765).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08367 Genomic DNA. Translation: CAA69654.1.
Y07817 Genomic DNA. Translation: CAA69151.1.
AE003852 Genomic DNA. Translation: AAF95717.1.
PIRiB82057.
RefSeqiNP_232204.1. NC_002505.1.
WP_000101599.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF95717; AAF95717; VC_2576.
GeneIDi2615593.
KEGGivch:VC2576.
PATRICi20084178. VBIVibCho83274_2455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08367 Genomic DNA. Translation: CAA69654.1.
Y07817 Genomic DNA. Translation: CAA69151.1.
AE003852 Genomic DNA. Translation: AAF95717.1.
PIRiB82057.
RefSeqiNP_232204.1. NC_002505.1.
WP_000101599.1. NC_002505.1.

3D structure databases

ProteinModelPortaliP78283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC2576.

Protocols and materials databases

DNASUi2615593.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF95717; AAF95717; VC_2576.
GeneIDi2615593.
KEGGivch:VC2576.
PATRICi20084178. VBIVibCho83274_2455.

Phylogenomic databases

eggNOGiENOG4105CGG. Bacteria.
COG0201. LUCA.
KOiK03076.
OMAiQTYVISQ.

Enzyme and pathway databases

BioCyciVCHO:VC2576-MONOMER.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY. 1 hit.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR030659. SecY_CS.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSECY_VIBCH
AccessioniPrimary (citable) accession number: P78283
Secondary accession number(s): Q9KP04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: September 7, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.